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Literature summary for 1.3.1.84 extracted from
- Acrylyl-coenzyme A reductase, an enzyme involved in the assimilation of 3-hydroxypropionate by Rhodobacter sphaeroides (2013), J. Bacteriol., 195, 4716-4725 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ATP | ATP-dependent | Cereibacter sphaeroides |  |
| ATP | ATP-dependent | Ruegeria pomeroyi | |
| ATP | ATP-dependent | Escherichia coli | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene RSP_1434, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3) | Cereibacter sphaeroides |
| gene SPO_1914, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), recombinant expression in Rhodobacter sphaeroides mutant DELTAacuI::kan complements 3-hydroxypropionate-dependent growth of the mutant strain | Ruegeria pomeroyi |
| gene yhdH, cloning and expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), recombinant expression in Rhodobacter sphaeroides mutant DELTAacuI::kan complements 3-hydroxypropionate-dependent growth of the mutant strain | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of mutant DELTAacuI::kan. The introduction of codon-optimized genes SPO_1914 or yhdH into the DELTAacuI::kan mutant of Rhodobacter sphaeroides on plasmid pMA5-1 complements 3-hydroxypropionate-dependent growth of the mutant strain | Cereibacter sphaeroides |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Cereibacter sphaeroides | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Ruegeria pomeroyi | |
| additional information | - |
additional information | Michaelis-Menten kinetics | Escherichia coli | |
| 0.0011 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Escherichia coli | |
| 0.0015 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Cereibacter sphaeroides | |
| 0.0028 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Ruegeria pomeroyi | |
| 0.018 | - |
NADPH | pH 7.0, 30°C, recombinant His-tagged enzyme | Ruegeria pomeroyi | |
| 0.028 | - |
NADPH | pH 7.0, 30°C, recombinant His-tagged enzyme | Cereibacter sphaeroides | |
| 0.033 | - |
NADPH | pH 7.0, 30°C, recombinant His-tagged enzyme | Escherichia coli | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Cereibacter sphaeroides | |
| Mg2+ | required | Ruegeria pomeroyi | |
| Mg2+ | required | Escherichia coli | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 56000 | - |
recombinant His10-tagged enzyme, gel filtration | Escherichia coli |
| 62000 | - |
recombinant His10-tagged enzyme, gel filtration | Ruegeria pomeroyi |
| 64000 | - |
recombinant His10-tagged enzyme, gel filtration | Cereibacter sphaeroides |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acrylyl-CoA + NADPH + H+ | Cereibacter sphaeroides | - |
propanoyl-CoA + NADP+ | - |
? | |
| acrylyl-CoA + NADPH + H+ | Ruegeria pomeroyi | - |
propanoyl-CoA + NADP+ | - |
? | |
| acrylyl-CoA + NADPH + H+ | Escherichia coli | - |
propanoyl-CoA + NADP+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cereibacter sphaeroides | Q3J6K9 | - |
- |
| Escherichia coli | P26646 | substrain MG1655 | - |
| Ruegeria pomeroyi | Q5LS56 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His10-tagged enzyme 11fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration | Cereibacter sphaeroides |
| recombinant His10-tagged enzyme 4fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration | Ruegeria pomeroyi |
| recombinant His10-tagged enzyme 6fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration | Escherichia coli |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | anoxygenic phototroph Rhodobacter sphaeroides uses 3-hydroxypropionate as a sole carbon source for growth | Cereibacter sphaeroides | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 72 | - |
pH 7.0, 30°C, purified recombinant His-tagged enzyme | Escherichia coli |
| 98 | - |
pH 7.0, 30°C, purified recombinant His-tagged enzyme | Ruegeria pomeroyi |
| 130 | - |
pH 7.0, 30°C, purified recombinant His-tagged enzyme | Cereibacter sphaeroides |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| acrylyl-CoA + NADH + H+ | - |
Cereibacter sphaeroides | propanoyl-CoA + NAD+ | - |
? | |
| acrylyl-CoA + NADH + H+ | - |
Ruegeria pomeroyi | propanoyl-CoA + NAD+ | - |
? | |
| acrylyl-CoA + NADH + H+ | - |
Escherichia coli | propanoyl-CoA + NAD+ | - |
? | |
| acrylyl-CoA + NADPH + H+ | - |
Cereibacter sphaeroides | propanoyl-CoA + NADP+ | - |
? | |
| acrylyl-CoA + NADPH + H+ | - |
Ruegeria pomeroyi | propanoyl-CoA + NADP+ | - |
? | |
| acrylyl-CoA + NADPH + H+ | - |
Escherichia coli | propanoyl-CoA + NADP+ | - |
? | |
| additional information | no activity with crotonyl-CoA. AcuI also does not catalyze reduction of acrylate or dehydration/reduction of 3-hydroxypropionyl-CoA | Cereibacter sphaeroides | ? | - |
? | |
| additional information | the enzyme shows a low but detectable activity for NADPH-dependent crotonyl-CoA reduction | Ruegeria pomeroyi | ? | - |
? | |
| additional information | the enzyme shows a low but detectable activity for NADPH-dependent crotonyl-CoA reduction | Escherichia coli | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 37000, about, recombinant His10-tagged enzyme, SDS-PAGE | Cereibacter sphaeroides |
| homodimer | 2 * 37000, about, recombinant His10-tagged enzyme, SDS-PAGE | Ruegeria pomeroyi |
| homodimer | 2 * 37000, about, recombinant His10-tagged enzyme, SDS-PAGE | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| acrylyl-CoA reductase | - |
Cereibacter sphaeroides |
| acrylyl-CoA reductase | - |
Ruegeria pomeroyi |
| acrylyl-CoA reductase | - |
Escherichia coli |
| acrylyl-coenzyme A reductase | - |
Cereibacter sphaeroides |
| acrylyl-coenzyme A reductase | - |
Ruegeria pomeroyi |
| acrylyl-coenzyme A reductase | - |
Escherichia coli |
| AcuI | - |
Cereibacter sphaeroides |
| AcuI | - |
Ruegeria pomeroyi |
| AcuI | - |
Escherichia coli |
| NADPH-dependent acrylyl-CoA reductase | - |
Cereibacter sphaeroides |
| NADPH-dependent acrylyl-CoA reductase | - |
Ruegeria pomeroyi |
| NADPH-dependent acrylyl-CoA reductase | - |
Escherichia coli |
| RSP_1434 | - |
Cereibacter sphaeroides |
| SPO_1914 | - |
Ruegeria pomeroyi |
| yhdH | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Cereibacter sphaeroides |
| 30 | - |
assay at | Ruegeria pomeroyi |
| 30 | - |
assay at | Escherichia coli |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 45 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Escherichia coli | |
| 60 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Ruegeria pomeroyi | |
| 80 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Cereibacter sphaeroides | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | broad optimum | Cereibacter sphaeroides |
| 7 | - |
assay at | Ruegeria pomeroyi |
| 7 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the catalytic efficiency for NADPH is 10fold higher compared to NADH | Escherichia coli | |
| additional information | the catalytic efficiency for NADPH is about 70fold higher compared to NADH | Ruegeria pomeroyi | |
| additional information | the catalytic efficiency for NADPH is more than 10fold higher compared to NADH | Cereibacter sphaeroides | |
| NADH | low activity | Cereibacter sphaeroides | |
| NADH | low activity | Ruegeria pomeroyi | |
| NADH | low activity | Escherichia coli | |
| NADPH | highly specific for | Cereibacter sphaeroides | |
| NADPH | highly specific for | Ruegeria pomeroyi | |
| NADPH | highly specific for | Escherichia coli | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Cereibacter sphaeroides | the enzyme is upregulated in cell extracts of Rhodobacter sphaeroides grown with 3-hydroxypropionate compared to those grown with succinate as a sole carbon source | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily | Cereibacter sphaeroides |
| evolution | the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily | Ruegeria pomeroyi |
| evolution | the enzyme belongs to the the MDR012 family of the medium-chain dehydrogenase/reductase (MDR) superfamily | Escherichia coli |
| malfunction | the introduction of codon-optimized SPO_1914 or yhdH into a DELTAacuI::kan mutant of Rhodobacter sphaeroides on a plasmid complements 3-hydroxypropionate-dependent growth. But in their native hosts, SPO_1914 and yhdH are believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate. Complementation of the DELTAacuI::kan mutant phenotype by crotonyl-CoA carboxylase/reductase from Rhodobacter sphaeroides is attributed to the fact that the fact that the enzyme also uses acrylyl-CoA as a substrate | Cereibacter sphaeroides |
| metabolism | enzyme SPO_1914 is believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate | Ruegeria pomeroyi |
| metabolism | enzyme yhdH is believed to function in the metabolism of substrates other than 3-hydroxypropionate, where acrylyl-CoA is an intermediate | Escherichia coli |
| metabolism | the enzyme is part of the proposed reductive pathway for 3-hydroxypropionate assimilation by Rhodobacter sphaeroides 2.4.1, overview | Cereibacter sphaeroides |
| physiological function | the enzyme is involved in 3-hydroxypropionate assimilation via the reductive conversion to propionyl-coenzyme A (CoA). Rhodobacter sphaeroides catalyzes the NADPH-dependent acrylyl-CoA reduction to produce propionyl-CoA. Reductive conversion of 3-hydroxypropionate to propionyl-CoA is a necessary route for assimilation of this C3 compound and ultimately supplies succinyl-CoA, a precursor metabolite required for cell carbon biosynthesis | Cereibacter sphaeroides |
| physiological function | the enzyme is involved in 3-hydroxypropionate assimilation via the reductive conversion to propionyl-coenzyme A (CoA). The plasmid-encoded, codon-optimized SPO_1914 enzyme, introduced of into a DELTAacuI::kan mutant of Rhodobacter sphaeroides, complements the 3-hydroxypropionate-dependent growth of the mutant | Ruegeria pomeroyi |
| physiological function | the enzyme is involved in 3-hydroxypropionate assimilation via the reductive conversion to propionyl-coenzyme A (CoA). The plasmid-encoded, codon-optimized yhdH enzyme, introduced of into a DELTAacuI::kan mutant of Rhodobacter sphaeroides, complements the 3-hydroxypropionate-dependent growth of the mutant | Escherichia coli |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 100 | - |
NADH | pH 7.0, 30°C, recombinant His-tagged enzyme | Ruegeria pomeroyi | |
| 270 | - |
NADH | pH 7.0, 30°C, recombinant His-tagged enzyme | Escherichia coli | |
| 420 | - |
NADH | pH 7.0, 30°C, recombinant His-tagged enzyme | Cereibacter sphaeroides | |
| 2700 | - |
NADPH | pH 7.0, 30°C, recombinant His-tagged enzyme | Escherichia coli | |
| 5700 | - |
NADPH | pH 7.0, 30°C, recombinant His-tagged enzyme | Cereibacter sphaeroides | |
| 6700 | - |
NADPH | pH 7.0, 30°C, recombinant His-tagged enzyme | Ruegeria pomeroyi | |
| 53333 | - |
acrylyl-CoA | pH 7.0, 30°C, recombinant His-tagged enzyme | Cereibacter sphaeroides | |
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